Functional homo- and heterodimeric actin capping proteins from the malaria parasite

DOI: 10.1016/j.bbrc.2020.02.119

Authors: Abris Adam Bendes (University of Oulu) , Moon Chatterjee (Helmholtz Centre for Infection Research; DESY) , Benjamin Götte (Helmholtz Centre for Infection Research; DESY) , Petri Kursula (University of Bergen) , Inari Kursula (University of Oulu; Helmholtz Centre for Infection Research; DESY; University of Bergen)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical And Biophysical Research Communications

State: Published (Approved)
Published: March 2020

Abstract: Actin capping proteins belong to the core set of proteins minimally required for actin-based motility and are present in virtually all eukaryotic cells. They bind to the fast-growing barbed end of an actin filament, preventing addition and loss of monomers, thus restricting growth to the slow-growing pointed end. Actin capping proteins are usually heterodimers of two subunits. The Plasmodium orthologs are an exception, as their α subunits are able to form homodimers. We show here that, while the β subunit alone is unstable, the α subunit of the Plasmodium actin capping protein forms functional homo- and heterodimers. This implies independent functions for the αα homo- and αβ heterodimers in certain stages of the parasite life cycle. Structurally, the homodimers resemble canonical αβ heterodimers, although certain rearrangements at the interface must be required. Both homo- and heterodimers bind to actin filaments in a roughly equimolar ratio, indicating they may also bind other sites than barbed ends.

Journal Keywords: Actin; Capping protein; Heterodimer; Homodimer; Malaria; Plasmodium

Diamond Keywords: Malaria

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: B21-High Throughput SAXS

Added On: 04/03/2020 09:06

Discipline Tags:

Pathogens Infectious Diseases Disease in the Developing World Health & Wellbeing Biochemistry Chemistry Life Sciences & Biotech Parasitology

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)